Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome.
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BBS genes are expressed exclusively in ciliated neurons in C. elegans
"all available Caenorhabditis elegans BBS homologues are expressed exclusively in ciliated neurons"
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BBS genes contain regulatory elements for RFX transcription factor
"contain regulatory elements for RFX, a transcription factor that modulates the expression of genes associated with ciliogenesis and intraflagellar transport"
Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport.
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bbs-7 and bbs-8 mutations cause structural and functional ciliary defects
"mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia"
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BBS proteins localize predominantly at the base of cilia and move bidirectionally along the ciliary axoneme
"C. elegans BBS proteins localize predominantly at the base of cilia, and like proteins involved in intraflagellar transport (IFT), a process necessary for cilia biogenesis and maintenance, move bidirectionally along the ciliary axoneme"
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BBS-7 and BBS-8 are required for normal IFT protein localization/motility
"BBS-7 and BBS-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris and CHE-11"
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BBS proteins play selective roles in IFT particle assembly and function
"We propose that BBS proteins play important, selective roles in the assembly and/or function of IFT particle components"
Mechanism of transport of IFT particles in C. elegans cilia by the concerted action of kinesin-II and OSM-3 motors.
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In bbs-7/bbs-8 mutants, IFT-A and IFT-B dissociate during anterograde transport
"in bbs-7/-8 mutants, kinesin-II and IFT-A move together at 0.5 μm/s, but OSM-3–kinesin and IFT-B move as a distinct complex at 1.3 μm/s"
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BBS-7/8 proteins coordinate IFT by holding IFT-A and IFT-B subcomplexes together
"BBS-7/-8 proteins coordinate IFT by holding subcomplexes IFT-A and -B together and stabilizing the integrity of the IFT particles"
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Loss of BBS-7 and -8 function leads to ciliary distal segment loss
"the loss of BBS-7 and -8 function in mutant animals leads to the loss of ciliary distal segments and sensory defects"
Endocytosis genes facilitate protein and membrane transport in C. elegans sensory cilia.
The BBSome controls IFT assembly and turnaround in cilia.
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BBSome assembles IFT complexes at the ciliary base and tip
"the BBSome is required for assembling IFT particles at both ciliary base and tip"
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BBS-1, BBS-7, and BBS-9 exist in the same complex (BiFC confirmation)
"fluorescence complementation can be observed in BBS-1–BBS-7 and BBS-1–BBS-9 pair, indicative of the coexistence of these three BBS proteins in the same complex"
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BBSome functions as scaffold for IFT-A, IFT-B, and IFT cargos
"the BBSome functions as a scaffold to organize IFT-A, IFT-B, ciliary membrane receptors, ciliary signaling molecules, and/or other IFT cargos into an entire unit and prepare it for IFT transport"
Ciliopathy proteins establish a bipartite signaling compartment in a C. elegans thermosensory neuron.
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BBS-8 and DAF-25 required for correct localization of guanylyl cyclases
"requires BBS-8 and DAF-25 (known as Ankmy2 in mammals) for correct localization of guanylyl cyclases needed for thermosensation"
Deep research report on bbs-7